Cerebral Bioenergetics and in Vivo Cytochrome c Oxidase Redox Relationships

1985 ◽  
pp. 815-821 ◽  
Author(s):  
A. L. Sylvia ◽  
C. A. Piantadosi ◽  
F. F. Jöbsis-Vander Vliet
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase

scholarly journals The isoforms of yeast cytochrome c oxidase subunit V alter the in vivo kinetic properties of the holoenzyme

1991 ◽  
Vol 266 (7) ◽  
pp. 4180-4186
Author(s):  
R A Waterland ◽  
A Basu ◽  
B Chance ◽  
R O Poyton
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Kinetic Properties ◽  
Oxidase Subunit

Exposure of Bacillus subtilis to silver inhibits activity of cytochrome c oxidase in vivo via interaction with SCO, the CuA assembly protein

Metallomics ◽  
2018 ◽  
Vol 10 (5) ◽  
pp. 735-744 ◽  
Author(s):  
Shina Hussain ◽  
Diann Andrews ◽  
Bruce C. Hill
Keyword(s):  
Bacillus Subtilis ◽  
Cytochrome C ◽  
Antimicrobial Agent ◽  
Cytochrome C Oxidase ◽  
Medicinal Use

Silver has long been used as an antimicrobial agent in general and medicinal use.

scholarly journals Cytochrome c oxidase III as a mechanism for apoptosis in heart failure following myocardial infarction

2009 ◽  
Vol 297 (4) ◽  
pp. C928-C934 ◽  
Author(s):  
Changgong Wu ◽  
Lin Yan ◽  
Christophe Depre ◽  
Sunil K. Dhar ◽  
You-Tang Shen ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Myocardial Infarction ◽  
Heart Failure ◽  
Cytochrome C ◽  
Protein Expression ◽  
Cell Viability ◽  
Cytochrome C Oxidase ◽  
Mitochondrial Gene

Cytochrome c oxidase (COX) is composed of 13 subunits, of which COX I, II, and III are encoded by a mitochondrial gene. COX I and II function as the main catalytic components, but the function of COX III is unclear. Because myocardial ischemia affects mitochondrial oxidative metabolism, we hypothesized that COX activity and expression would be affected during postischemic cardiomyopathy. This hypothesis was tested in a monkey model following myocardial infarction (MI) and subsequent pacing-induced heart failure (HF). In this model, COX I protein expression was decreased threefold after MI and fourfold after HF ( P < 0.05 vs. sham), whereas COX II expression remained unchanged. COX III protein expression increased 5-fold after MI and further increased 10-fold after HF compared with sham ( P < 0.05 vs. sham). The physiological impact of COX III regulation was examined in vitro. Overexpression of COX III in mitochondria of HL-1 cells resulted in an 80% decrease in COX I, 60% decrease in global COX activity, 60% decrease in cell viability, and threefold increase in apoptosis ( P < 0.05). Oxidative stress induced by H2O2 significantly ( P < 0.05) increased COX III expression. H2O2 decreased cell viability by 47 ± 3% upon overexpression of COX III, but only by 12 ± 5% in control conditions ( P < 0.05). We conclude that ischemic stress in vivo and oxidative stress in vitro lead to upregulation of COX III, followed by downregulation of COX I expression, impaired COX oxidative activity, and increased apoptosis. Therefore, upregulation of COX III may contribute to the increased susceptibility to apoptosis following MI and subsequent HF.

Effect of illumination on the redox state of cytochrome c oxidase in wheat leaves in vivo

1986 ◽  
Vol 5 (4) ◽  
pp. 259-261 ◽  
Author(s):  
M. S. Naik ◽  
J. D. Nicholas
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Redox State ◽  
Wheat Leaves

Chronic In Vivo Sodium Azide Infusion Induces Selective and Stable Inhibition of Cytochrome c Oxidase

2002 ◽  
Vol 66 (6) ◽  
pp. 2606-2611 ◽  
Author(s):  
M. Catherine Bennett ◽  
Gary W. Mlady ◽  
Young-Hwa Kwon ◽  
Gregory M. Rose
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Sodium Azide

Mitochondrial Protein Content and in Vivo Synthesis Rates in Skeletal Muscle from Critically Ill Rats

1996 ◽  
Vol 91 (4) ◽  
pp. 475-481 ◽  
Author(s):  
Olav E. Rooyackers ◽  
Alexande R H. Kersten ◽  
Anton J. M. Wagenmakers
Keyword(s):  
Skeletal Muscle ◽  
Critical Illness ◽  
Cytochrome C ◽  
Protein Content ◽  
Cytochrome C Oxidase ◽  
Citrate Synthase ◽  
Mitochondrial Protein ◽  
Substantial Reduction ◽  
Mitochondrial Content

1. Recently we reported decreased activities of two mitochondrial marker enzymes (citrate synthase and cytochrome c oxidase) in skeletal muscle from a rat model of critical illness (zymosan injection). In the present study we investigated (i) whether these decreases in enzyme activity reflect a reduction in mitochondrial content and (ii) whether this potential reduction in mitochondrial content was the result of decreased mitochondrial protein synthesis rates. 2. Mitochondrial protein content was calculated from the activities of cytochrome c oxidase in whole-muscle homogenates and purified mitochondria. Synthesis rates of mitochondrial protein in vivo were studied by measuring the incorporation of [3H]phenylalanine into mitochondrial protein using the flooding dose technique. 3. Mitochondrial protein content was reduced to 54% of that measured in the pair-fed rats and to 71% of that measured in control rats fed ad libitum 2 days after the zymosan treatment The decreased mitochondrial protein content observed 2 days after zymosan challenge was preceded by a reduced rate of synthesis of mitochondrial protein 16 h after treatment. Both changes were of greater magnitude than the general muscle wasting and the decreased rate of synthesis of mixed protein observed in the zymosan-treated rats. 4. We conclude that the acute phase of critical illness in zymosan-treated rats is characterized by a substantial reduction in muscle mitochondria that is at least in part caused by a decreased rate of synthesis of mitochondrial protein. This derangement in mitochondrial protein metabolism may be related to the impaired muscle function observed during and after critical illness.

Reduction of cytochrome-c oxidase copper precedes failing cerebral O2 utilization in fluorocarbon-perfused cats

1996 ◽  
Vol 271 (2) ◽  
pp. H579-H587 ◽  
Author(s):  
R. Stingele ◽  
B. Wagner ◽  
M. V. Kameneva ◽  
M. A. Williams ◽  
D. A. Wilson ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Redox State ◽  
Near Infrared ◽  
Hypoxic Conditions ◽  
Sagittal Sinus ◽  
Tissue Po2 ◽  
Relationship Of ◽  
The Relationship

We determined the relationship of the low-potential copper (CuA) redox state of cytochrome-c oxidase to the brain tissue PO2 (PtiO2) and global cerebral O2 consumption (CMRO2) in vivo. The redox state of cytochrome-c oxidase copper was monitored in perfluorocarbon-exchanged cats under normoxic and graded hypoxic conditions with use of near-infrared spectroscopy. Continuous spectra ranging from 730 to 960 nm were acquired, and the change in copper redox state was assessed by the absorption changes at 830 nm. PtiO2 was measured with O2-sensitive electrodes implanted into the cortex, and CMRO2 was determined by sampling arterial and superior sagittal sinus perfusate and by measuring blood flow with radiolabeled microspheres. As PtiO2 decreased with hypoxia, the CuA of cytochrome-c oxidase became progressively reduced, whereas the CMRO2 was unchanged during the initial stages of hypoxia. Only with severe hypoxia, did CMRO2 and the amplitude of somatosensory evoked potentials decrease. We conclude that the CuA site of cytochrome-c oxidase is involved in a regulatory adjustment that helps maintain CMRO2 constant.

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